JOURNAL of the JAPAN RESEARCH ASSOCIATION for TEXTILE END-USES
Online ISSN : 1884-6599
Print ISSN : 0037-2072
ISSN-L : 0037-2072
Volume 29, Issue 4
Displaying 1-6 of 6 articles from this issue
  • [in Japanese]
    1988 Volume 29 Issue 4 Pages 124-132
    Published: April 25, 1988
    Released on J-STAGE: September 30, 2010
    JOURNAL FREE ACCESS
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  • [in Japanese]
    1988 Volume 29 Issue 4 Pages 133-136
    Published: April 25, 1988
    Released on J-STAGE: September 30, 2010
    JOURNAL FREE ACCESS
    Download PDF (647K)
  • [in Japanese], [in Japanese]
    1988 Volume 29 Issue 4 Pages 141-145
    Published: April 25, 1988
    Released on J-STAGE: September 30, 2010
    JOURNAL FREE ACCESS
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  • Part 7 : Oily Soil Removal in the Formulation of Protease and Lipase
    Masako Sato, Junko Ohe, Yasuko Nishida, Motoi Minagawa
    1988 Volume 29 Issue 4 Pages 146-154
    Published: April 25, 1988
    Released on J-STAGE: September 30, 2010
    JOURNAL FREE ACCESS
    Using the phosphate-free detergents formulated with protease and lipase, the effects of stability of lipolytic enzyme, lipase, in the washing solution on the removal of oily soils from cotton fabric were investigated at pH 9.5, 30°C.
    1) Activities of two kinds of lipases originated from Rhizopus and Mucor, were reduced by anionic surfactants, and stabilized by adding nonionic polymers.
    2) The removal of oleic acid and triolein were promoted in the solution of sodium sulfite as an alkaline reduction agent.
    3) Nonpolar triolein was removed effectively in lipase solution containing reducing agent and PVA caused by their synergistic effects.
    4) In the model formulations of detergent, protease/lipase/DBS systems, oily soils were removed not only by the actions of hydrolysis of lipase but also by those of synergistic effects caused by interactions between oily soils and other soil, such as protein, on the fabric, and by interactions between the soils and formulated compounds.
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  • Part 8 : Protein Soil Removal in the Formulation of Protease and Lipase
    Masako Sato, Kenichi Yoshikawa, Naoko Kitamura, Motoi Minagawa
    1988 Volume 29 Issue 4 Pages 155-161
    Published: April 25, 1988
    Released on J-STAGE: September 30, 2010
    JOURNAL FREE ACCESS
    Using the phosphate-free detergents formulated with protease and lipase, the effects of stability of protease in the washing solution on removal of protein soils from cotton fabric were investigated at pH9.5, 30°C.
    1) Effect of PVA on stabilities of protease activity in the solutions containing anionic surfactant; DBS, was recognized markedly, but on the removal of gelatin from cotton fabric was not so effective compared with stabilized activity.
    2) Addition of Ca2+ to protease was recognized more effectively than addition of PVA not only on activity but also on gelatin soil removal.
    3) In the washing liquor containing various compounds, protein soil removal by hydrolysis was influenced by adsorption of protease-compound complex.
    4) In the model formulations of detergent, protease/lipase/DBS systems, protein in mixed soil with oils and fats was removed effectively not only by the actions of hydrolysis by protease but also by lipase hydrolysis because of synergistic effects.
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  • Part 1: A proposal of the Instrumental Evaluating Equation on Light Fastness
    Kazushige Teraji, Tetsuya Sato
    1988 Volume 29 Issue 4 Pages 162-166
    Published: April 25, 1988
    Released on J-STAGE: September 30, 2010
    JOURNAL FREE ACCESS
    The instrumental method for assessing the light fastness of colored materials was investigated by analyzing the color change of the wool blue standard specimens by exposure to carbon-arc light.
    The following equation was obtained from the relation between exposure time to light and the color change indices Nc# of the wool blue standard specimens.
    NL=ln { (5.5-Nc#) / (FL×T1/n) } / (ln KL)
    where, NL: light fastness value in accordance with the blue standard numbers
    Nc#: the color change index assessed in accordance with the gray scale rating
    FL: criterion constant of assessment of light fastness
    T: exposured time in hours
    n: power number determined with KL
    KL: light exposure time constant
    This method is expected to supersede the present subjective visual method for assessing the light fastness.
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